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Database: UniProt
Entry: A0A011QCF7_9PROT
LinkDB: A0A011QCF7_9PROT
Original site: A0A011QCF7_9PROT 
ID   A0A011QCF7_9PROT        Unreviewed;       483 AA.
AC   A0A011QCF7;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000256|ARBA:ARBA00019702};
DE            EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287};
GN   Name=cbbM {ECO:0000313|EMBL:EXI76444.1};
GN   ORFNames=AW07_00392 {ECO:0000313|EMBL:EXI76444.1};
OS   Candidatus Accumulibacter sp. SK-11.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=1454000 {ECO:0000313|EMBL:EXI76444.1, ECO:0000313|Proteomes:UP000020226};
RN   [1] {ECO:0000313|EMBL:EXI76444.1, ECO:0000313|Proteomes:UP000020226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK-11 {ECO:0000313|Proteomes:UP000020226};
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC       ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC       fixation, as well as the oxidative fragmentation of the pentose
CC       substrate. Both reactions occur simultaneously and in competition at
CC       the same active site. {ECO:0000256|ARBA:ARBA00003617}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type II
CC       subfamily. {ECO:0000256|ARBA:ARBA00005475}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXI76444.1}.
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DR   EMBL; JFAW01000002; EXI76444.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A011QCF7; -.
DR   SMR; A0A011QCF7; -.
DR   STRING; 1454000.AW07_00392; -.
DR   PATRIC; fig|1454000.3.peg.328; -.
DR   Proteomes; UP000020226; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR   CDD; cd08211; RuBisCO_large_II; 1.
DR   Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 1.
DR   HAMAP; MF_01339; RuBisCO_L_type2; 1.
DR   InterPro; IPR033966; RuBisCO.
DR   InterPro; IPR020878; RuBisCo_large_chain_AS.
DR   InterPro; IPR000685; RuBisCO_lsu_C.
DR   InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR   InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR   InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR   InterPro; IPR020871; RuBisCO_lsuII.
DR   PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR   PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR   SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1.
DR   PROSITE; PS00157; RUBISCO_LARGE; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:EXI76444.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020226}.
FT   DOMAIN          37..154
FT                   /note="Ribulose bisphosphate carboxylase large subunit
FT                   ferrodoxin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02788"
FT   DOMAIN          167..464
FT                   /note="Ribulose bisphosphate carboxylase large subunit C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00016"
SQ   SEQUENCE   483 AA;  53305 MW;  05938153556F34BD CRC64;
     MLPGRTPAAQ LKLTILHIDA RENNMDQSNR YADLSLREED LIAGGKHILV AYKMKPKAGY
     DYLPAAAHFA AESSTGTNVE VSTTDDFTRG VDALVYQIDE ASEEMRIAYP LELFDRNVTD
     GRMMIVSFLT LCIGNNQGMG DIEHAKIYDF HVPERALQLF DGPAKDISDL WRILGRPIRD
     GGYIAGTIIK PKLGLRPEPF ALAAYQFWLG GDFIKNDEPQ GNQVFAPMKK VMPLVYDAMK
     RAQDETGQAK IFSANITADD HCEMCARADY ILETFGPDAD KVAFLVDGYV GGPGMVTTAR
     RQYPNQYLHY HRAGHGAVTS PSSKRGYTAY VLAKMARLQG ASGIHVGTMG FGKMEGDADD
     RAIAYIIERD EYQGPAYYQK WYGMKPTTPI ISGGMNALRL PGFFANLGHG NVINTAGGGS
     YGHIDSPAAG AISLRQAYEC WKAGADPIEW AREHREFARA FESFPGDADM LHPGWRDRLG
     AHR
//
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